2k1j

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File:2k1j.jpg

Template:STRUCTURE 2k1j

Plan homeodomain finger of tumour supressor ING4


OverviewOverview

Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4.

About this StructureAbout this Structure

2K1J is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2jmq. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4., Palacios A, Garcia P, Padro D, Lopez-Hernandez E, Martin I, Blanco FJ, FEBS Lett. 2006 Dec 22;580(30):6903-8. Epub 2006 Nov 30. PMID:17157298 Page seeded by OCA on Wed Apr 16 23:02:55 2008

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